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Characterization of a GH36 β-L-Arabinopyranosidase in Bifidobacterium adolescentis.

ABSTRACT: β-L-Arabinopyranosidases are classified into the glycoside hydrolase family 27 (GH27) and GH97, but not into GH36. In this study, we first characterized the GH36 β-L-arabinopyranosidase BAD_1528 from Bifidobacterium adolescentis JCM1275. The recombinant BAD_1528 expressed in Escherichia coli had a hydrolytic activity toward p-nitrophenyl (pNP)-β-L-arabinopyranoside (Arap) and a weak activity toward pNP-α-D-galactopyranoside (Gal). The enzyme liberated L-arabinose efficiently not from any oligosaccharides or polysaccharides containing Arap-β1,3-linkages, but from the disaccharide Arap-β1,3-L-arabinose. However, we were unable to confirm the in vitro fermentability of Arap-β1,3-Ara in B. adolescentis strains. The enzyme also had a transglycosylation activity toward 1-alkanols and saccharides as acceptors.

SUBMITTER: Sasaki Y

PROVIDER: S-EPMC8056906 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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Characterization of a GH36 β-L-Arabinopyranosidase in Bifidobacterium adolescentis.

Sasaki Yuki Y Togo Nami N Kitahara Kanefumi K Fujita Kiyotaka K

Journal of applied glycoscience 20180520 2

β-L-Arabinopyranosidases are classified into the glycoside hydrolase family 27 (GH27) and GH97, but not into GH36. In this study, we first characterized the GH36 β-L-arabinopyranosidase BAD_1528 from Bifidobacterium adolescentis JCM1275. The recombinant BAD_1528 expressed in Escherichia coli had a hydrolytic activity toward p-nitrophenyl (pNP)-β-L-arabinopyranoside (Arap) and a weak activity toward pNP-α-D-galactopyranoside (Gal). The enzyme liberated L- ...[more]

PMID: 34354509

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Characterization of recombinant beta-fructofuranosidase from Bifidobacterium adolescentis G1.

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